ID   ODPA_KLULA              Reviewed;         412 AA.
AC   O13366; Q6CKB5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   Name=PDA1; OrderedLocusNames=KLLA0F12001g;
OS   Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC MYA-539 / JBD100;
RX   MEDLINE=99098705; PubMed=9884236;
RA   Zeeman A.-M., Luttik M.A.H., Thiele C., van Dijken J.P., Pronk J.T.,
RA   Steensma H.Y.;
RT   "Inactivation of the Kluyveromyces lactis KlPDA1 gene leads to loss of
RT   pyruvate dehydrogenase activity, impairs growth on glucose and
RT   triggers aerobic alcoholic fermentation.";
RL   Microbiology 144:3437-3446(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- ENZYME REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha
CC       subunit (By similarity).
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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DR   EMBL; AF023920; AAD03773.1; -; Genomic_DNA.
DR   EMBL; CR382126; CAG98332.1; -; Genomic_DNA.
DR   RefSeq; XP_455624.1; -.
DR   HSSP; P08559; 1NI4.
DR   GeneID; 2894999; -.
DR   KEGG; kla:KLLA0F12001g; -.
DR   HOGENOM; O13366; -.
DR   OMA; O13366; LEYETYR.
DR   BRENDA; 1.2.4.1; 74088.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    412       Pyruvate dehydrogenase E1 component
FT                                subunit alpha, mitochondrial.
FT                                /FTId=PRO_0000020450.
FT   CONFLICT    275    281       YQASKFA -> TKL (in Ref. 1; AAD03773).
SQ   SEQUENCE   412 AA;  45453 MW;  CBCC8AB3DC4C7E96 CRC64;
     MLSLKAQSSV VGKSSSLRLV RNFSKNVRAL SQVADETKPG DDDLVQIDLP ETSFEGYLLD
     VPELSYQTTK SNLLQMYKDM IIVRRMEMAC DALYKAKKIR GFCHSSVGQE AIAVGIENAI
     TKRDTVITSY RCHGFTYMRG AAVQAVLAEL MGRRTGVSFG KGGSMHLYAP GFYGGNGIVG
     AQVPLGAGLA FAHQYKHEDA CSFALYGDGA SNQGQVFESF NMAKLWNLPA VFCCENNKYG
     MGTAAARSSA MTEYFKRGQY IPGLKVNGMD ILAVYQASKF AKDWTVSGNG PIVLEYETYR
     YGGHSMSDPG TTYRTRDEIQ HMRSKNDPIA GLKMHLLELG IATEDEIKAY DKAARKYVDE
     QVELADAAPA PEAKMSILFE DVYVPGSETP TLRGRLQEDT WDFAKKSFAF RD
//